메뉴 건너뛰기




Volumn 103, Issue 1, 2002, Pages 26-35

Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease

Author keywords

Epitope; Extraneuronal; Intraneuronal; Neurofibrillary tangle; Pretangle

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; TAU PROTEIN;

EID: 0036937699     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004010100423     Document Type: Article
Times cited : (806)

References (57)
  • 1
    • 0034730759 scopus 로고    scopus 로고
    • Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation
    • Ackmann M, Wiech H, Mandelkow E (2000) Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation. J Biol Chem 275:30335-30343
    • (2000) J. Biol. Chem. , vol.275 , pp. 30335-30343
    • Ackmann, M.1    Wiech, H.2    Mandelkow, E.3
  • 3
    • 0025717816 scopus 로고
    • The topographical and neuroanatomical distribution of neurofibrillary tangles and neuritic plaques in the cerebral cortex of patients with Alzheimer's disease
    • Arnold SE, Hyman BT, Flory J, Damasio AR, Van Hoesen GW (1991) The topographical and neuroanatomical distribution of neurofibrillary tangles and neuritic plaques in the cerebral cortex of patients with Alzheimer's disease. Cereb Cortex 1:103-116
    • (1991) Cereb. Cortex , vol.1 , pp. 103-116
    • Arnold, S.E.1    Hyman, B.T.2    Flory, J.3    Damasio, A.R.4    Van Hoesen, G.W.5
  • 4
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada PV, Growdon JH, Hedley-Whyte ET, Hyman BT (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42: 631-639
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 5
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • Baumann K, Mandelkow EM, Biernat J, Piwnica-Worms H, Mandelkow E (1993) Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett 336:417-424
    • (1993) FEBS Lett. , vol.336 , pp. 417-424
    • Baumann, K.1    Mandelkow, E.M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 6
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J, Gustke N, Drewes G, Mandelkow EM, Mandelkow E (1993) Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11:153-163
    • (1993) Neuron. , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 7
    • 0032935412 scopus 로고    scopus 로고
    • The development of cell processes induced by tau protein requires phosphorylation of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains
    • Biernat J, Mandelkow EM (1999) The development of cell processes induced by tau protein requires phosphorylation of serine 262 and 356 in the repeat domain and is inhibited by phosphorylation in the proline-rich domains. Mol Biol Cell 10:727-740
    • (1999) Mol. Biol. Cell , vol.10 , pp. 727-740
    • Biernat, J.1    Mandelkow, E.M.2
  • 9
    • 0023111344 scopus 로고
    • Argyrophilic grains: Characteristic pathology of cerebral cortex in cases of adult onset dementia without Alzheimer changes
    • Braak H, Braak E (1987) Argyrophilic grains: characteristic pathology of cerebral cortex in cases of adult onset dementia without Alzheimer changes. Neurosci Lett 76:124-127
    • (1987) Neurosci. Lett. , vol.76 , pp. 124-127
    • Braak, H.1    Braak, E.2
  • 10
    • 0024518532 scopus 로고
    • Cortical and subcortical argyrophilic grains characterize a disease associated with adult onset dementia
    • Braak H, Braak E (1989) Cortical and subcortical argyrophilic grains characterize a disease associated with adult onset dementia. Neuropathol Appl Neurobiol 15:13-26
    • (1989) Neuropathol. Appl. Neurobiol. , vol.15 , pp. 13-26
    • Braak, H.1    Braak, E.2
  • 11
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82:239-259
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 12
    • 0028364256 scopus 로고
    • Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation
    • Brandt R, Lee G, Teplow DB, Shalloway D, Abdel-Ghany M (1994) Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation. J Biol Chem 269:11776-11782
    • (1994) J. Biol. Chem. , vol.269 , pp. 11776-11782
    • Brandt, R.1    Lee, G.2    Teplow, D.B.3    Shalloway, D.4    Abdel-Ghany, M.5
  • 13
    • 0024348594 scopus 로고
    • The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer's disease
    • Crowther T, Goedert M, Wischik CM (1989) The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer's disease. Ann Med 21:127-132
    • (1989) Ann. Med. , vol.21 , pp. 127-132
    • Crowther, T.1    Goedert, M.2    Wischik, C.M.3
  • 14
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • Crowther RA, Olesen OF, Jakes R, Goedert M (1992) The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease. FEBS Lett 309:199-202
    • (1992) FEBS Lett. , vol.309 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 16
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E (1997) MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89:297-308
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 17
    • 0028937631 scopus 로고
    • Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262
    • Drewes G, Trinczek B, Illenberger S, Biernat J, Schmitt-Ulms G, Meyer HE, Mandelkow EM, Mandelkow E (1995) Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J Biol Chem 270: 7679-7688
    • (1995) J. Biol. Chem. , vol.270 , pp. 7679-7688
    • Drewes, G.1    Trinczek, B.2    Illenberger, S.3    Biernat, J.4    Schmitt-Ulms, G.5    Meyer, H.E.6    Mandelkow, E.M.7    Mandelkow, E.8
  • 18
    • 0032987650 scopus 로고    scopus 로고
    • Phosphorylation of tau protein by recombinant GSK-3beta: Pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain
    • Godemann R, Biernat J, Mandelkow E, Mandelkow EM (1999) Phosphorylation of tau protein by recombinant GSK-3beta: pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain. FEBS Lett 454:157-164
    • (1999) FEBS Lett. , vol.454 , pp. 157-164
    • Godemann, R.1    Biernat, J.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 19
    • 0027420369 scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease
    • Goedert M (1993) Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends Neurosci 16:460-465
    • (1993) Trends Neurosci. , vol.16 , pp. 460-465
    • Goedert, M.1
  • 20
    • 0024414440 scopus 로고
    • Amyloid plaques, neurofibrillary tangles and their relevance for the study of Alzheimer's disease
    • 405-406
    • Goedert M, Crowther RA (1989) Amyloid plaques, neurofibrillary tangles and their relevance for the study of Alzheimer's disease. Neurobiol Aging 10:405-406; 412-414
    • (1989) Neurobiol. Aging , vol.10 , pp. 412-414
    • Goedert, M.1    Crowther, R.A.2
  • 21
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M, Jakes R, Crowther RA, Cohen P, Vanmechelen E, Vandermeeren M, Cras P (1994) Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem J 301:871-877
    • (1994) Biochem. J. , vol.301 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3    Cohen, P.4    Vanmechelen, E.5    Vandermeeren, M.6    Cras, P.7
  • 22
    • 0028885494 scopus 로고
    • Protein phosphatase 2 A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase
    • Goedert M, Jakes R, Qi Z, Wang JH, Cohen P (1995) Protein phosphatase 2 A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase. J Neurochem 65:2804-2807
    • (1995) J. Neurochem. , vol.65 , pp. 2804-2807
    • Goedert, M.1    Jakes, R.2    Qi, Z.3    Wang, J.H.4    Cohen, P.5
  • 23
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert M, Jakes R, Vanmechelen E (1995) Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci Lett 189:167-169
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-169
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 24
    • 0026231697 scopus 로고
    • Neurofibrillary tangles and beta-amyloid deposits in Alzheimer's disease
    • Goedert M, Sisodia SS, Price DL (1991) Neurofibrillary tangles and beta-amyloid deposits in Alzheimer's disease. Curr Opin Neurobiol 1:441-447
    • (1991) Curr. Opin. Neurobiol. , vol.1 , pp. 441-447
    • Goedert, M.1    Sisodia, S.S.2    Price, D.L.3
  • 25
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert M, Wischik CM, Crowther RA, Walker JE, Klug A (1988) Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc Natl Acad Sci USA 85:4051-4055
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 26
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg SG, Davies P (1990) A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci USA 87:5827-5831
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 27
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau
    • Greenberg SG, Davies P, Schein JD, Binder LI (1992) Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J Biol Chem 267:564-569
    • (1992) J. Biol. Chem. , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 28
    • 0029879046 scopus 로고    scopus 로고
    • Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau protein
    • Hasegawa M, Jakes R, Crowther RA, Lee VM, Ihara Y, Goedert M (1996) Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau protein. FEBS Lett 384:25-30
    • (1996) FEBS Lett. , vol.384 , pp. 25-30
    • Hasegawa, M.1    Jakes, R.2    Crowther, R.A.3    Lee, V.M.4    Ihara, Y.5    Goedert, M.6
  • 29
    • 0030750558 scopus 로고    scopus 로고
    • Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites
    • Hoffmann R, Lee VMY, Leight S, Varga I, Otvos L Jr (1997) Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites. Biochemistry 36:8114-8124
    • (1997) Biochemistry , vol.36 , pp. 8114-8124
    • Hoffmann, R.1    Lee, V.M.Y.2    Leight, S.3    Varga, I.4    Otvos L., Jr.5
  • 30
    • 0014276827 scopus 로고
    • The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and "rod-like" structures as seen in Guam amyotrophic lateral sclerosis and parkinsonism-dementia complex
    • Hirano A, Dembitzer HM, Kurland LT, Zimmerman HM (1968) The fine structure of some intraganglionic alterations. Neurofibrillary tangles, granulovacuolar bodies and "rod-like" structures as seen in Guam amyotrophic lateral sclerosis and parkinsonism-dementia complex. J Neuropathol Exp Neurol 27:167-182
    • (1968) J. Neuropathol. Exp. Neurol. , vol.27 , pp. 167-182
    • Hirano, A.1    Dembitzer, H.M.2    Kurland, L.T.3    Zimmerman, H.M.4
  • 32
    • 0029965781 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics
    • Illenberger S, Drewes G, Trinczek B, Biernat J, Meyer HE, Olmsted JB, Mandelkow EM, Mandelkow E (1996) Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. J Biol Chem 271:10834-10843
    • (1996) J. Biol. Chem. , vol.271 , pp. 10834-10843
    • Illenberger, S.1    Drewes, G.2    Trinczek, B.3    Biernat, J.4    Meyer, H.E.5    Olmsted, J.B.6    Mandelkow, E.M.7    Mandelkow, E.8
  • 34
    • 0030783142 scopus 로고    scopus 로고
    • A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease
    • Jicha GA, Lane E, Vincent I, Otvos L, Jr., Hoffmann R, Davies P (1997) A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J Neurochem 69:2087-2095
    • (1997) J. Neurochem. , vol.69 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3    Otvos L., Jr.4    Hoffmann, R.5    Davies, P.6
  • 35
    • 0028904293 scopus 로고
    • Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein
    • Jou YS, Myers RM (1995) Evidence from antibody studies that the CAG repeat in the Huntington disease gene is expressed in the protein. Hum Mol Genet 4:465-469
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 465-469
    • Jou, Y.S.1    Myers, R.M.2
  • 36
    • 0022414054 scopus 로고
    • Diagnosis of Alzheimer's disease
    • Khachaturian ZS (1985) Diagnosis of Alzheimer's disease. Arch Neurol 42:1097-1105
    • (1985) Arch. Neurol. , vol.42 , pp. 1097-1105
    • Khachaturian, Z.S.1
  • 38
    • 0032851485 scopus 로고    scopus 로고
    • Demonstration by fluorescence resonance energy transfer of a close association between activated MAP kinase and neurofibrillary tangles: Implications for MAP kinase activation in Alzheimer disease
    • Knowles RB, Chin J, Ruff CT, Hyman BT (1999) Demonstration by fluorescence resonance energy transfer of a close association between activated MAP kinase and neurofibrillary tangles: implications for MAP kinase activation in Alzheimer disease. J Neuropathol Exp Neurol 58:1090-1098
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 1090-1098
    • Knowles, R.B.1    Chin, J.2    Ruff, C.T.3    Hyman, B.T.4
  • 39
    • 0026611728 scopus 로고
    • Immunological and conformation characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease
    • Lang E, Szendrei GI, Lee VM, Otvos L Jr (1992) Immunological and conformation characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease. Biochem Biophys Res Commun 187:783-790
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 783-790
    • Lang, E.1    Szendrei, G.I.2    Lee, V.M.3    Otvos L., Jr.4
  • 41
    • 0029899091 scopus 로고    scopus 로고
    • Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356
    • Litersky JM, Johnson GV, Jakes R, Goedert M, Lee M, Seubert P (1996) Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356. Biochem J 316:655-660
    • (1996) Biochem. J. , vol.316 , pp. 655-660
    • Litersky, J.M.1    Johnson, G.V.2    Jakes, R.3    Goedert, M.4    Lee, M.5    Seubert, P.6
  • 47
    • 0031468274 scopus 로고    scopus 로고
    • Neuropathological assessment of Alzheimer's disease: The experience of the Consortium to Establish a Registry for Alzheimer's Disease
    • 263-268
    • Mirra SS (1997) Neuropathological assessment of Alzheimer's disease: the experience of the Consortium to Establish a Registry for Alzheimer's Disease. Int Psychogeriatr 9:263-268;269-272
    • (1997) Int. Psychogeriatr. , vol.9 , pp. 269-272
    • Mirra, S.S.1
  • 48
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, Vogel FS, Hughes JP, van Belle G, Berg L (1991) The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 41:479-486
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6    Vogel, F.S.7    Hughes, J.P.8    van Belle, G.9    Berg, L.10
  • 50
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L Jr, Feiner L, Lang E, Szendrei GI, Goedert M, Lee VM (1994) Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J Neurosci Res 39:669-673
    • (1994) J. Neurosci. Res. , vol.39 , pp. 669-673
    • Otvos L., Jr.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.6
  • 53
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A, Biernat J, von Bergen M, Mandelkow E, Mandelkow EM (1999) Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38:3549-3558
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 55
    • 0028981873 scopus 로고
    • Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells
    • Sperber BR, Leight S, Goedert M, Lee VM (1995) Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells. Neurosci Lett 197:149-153
    • (1995) Neurosci. Lett. , vol.197 , pp. 149-153
    • Sperber, B.R.1    Leight, S.2    Goedert, M.3    Lee, V.M.4
  • 56
    • 0025093173 scopus 로고
    • Phosphorylation characteristics of the A68 protein in Alzheimer's disease
    • Vincent IJ, Davies P (1990) Phosphorylation characteristics of the A68 protein in Alzheimer's disease. Brain Res 531:127-135
    • (1990) Brain Res. , vol.531 , pp. 127-135
    • Vincent, I.J.1    Davies, P.2
  • 57
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Zheng-Fischhofer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E (1998) Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur J Biochem 252:542-552
    • (1998) Eur. J. Biochem. , vol.252 , pp. 542-552
    • Zheng-Fischhofer, Q.1    Biernat, J.2    Mandelkow, E.M.3    Illenberger, S.4    Godemann, R.5    Mandelkow, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.